Characterization of the oligosaccharide moiety of VIP receptor from the human pancreatic cell line BxPC-3

Peptides. 1993 Nov-Dec;14(6):1331-8. doi: 10.1016/0196-9781(93)90194-l.

Abstract

The human pancreatic cell line BxPC-3 displays two classes of binding sites with high and low affinity for VIP. The order of potency of VIP-related peptides in inhibiting either [125I]VIP or [125I]N-AcPACAP27 binding and in stimulating cAMP production was typical of the human VIP receptor. By combining affinity labeling with glycosidase treatments, we have characterized the VIP receptor as a M(r) = 68,200 glycoprotein, consisting of a M(r) = 39,300 polypeptide core with at least three N-linked oligosaccharide chains. In addition, our results revealed the presence of a low amount of sialic acid residues in the carbohydrate moiety of receptor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenocarcinoma / chemistry*
  • Glycoproteins / chemistry*
  • Humans
  • Oligosaccharides / analysis
  • Pancreatic Neoplasms / chemistry*
  • Radioligand Assay
  • Receptors, Vasoactive Intestinal Peptide / chemistry*
  • Tumor Cells, Cultured

Substances

  • Glycoproteins
  • Oligosaccharides
  • Receptors, Vasoactive Intestinal Peptide